Oxyl and hydroxyl radical transfer in mitochondrial amidoxime reducing component-catalyzed nitrite reduction.

ABSTRACT: A combination of electron paramagnetic resonance (EPR) spectroscopy and computational approaches has provided insight into the nature of the reaction coordinate for the one-electron reduction of nitrite by the mitochondrial amidoxime reducing component (mARC) enzyme. The results show that a paramagnetic Mo(V) species is generated when reduced enzyme is exposed to nitrite, and an analysis of the resulting EPR hyperfine parameters confirms that mARC is remarkably similar to the low-pH form of sulfite oxidase. Two mechanisms for nitrite reduction have been considered. The first shows a modest reaction barrier of 14 kcal/mol for the formation of ·NO from unprotonated nitrite substrate. In marked contrast, protonation of the substrate oxygen proximal to Mo in the Mo(IV)-O-N-O substrate-bound sp

SUBMITTER: Yang J 

PROVIDER: S-EPMC4872596 | biostudies-literature | 2015 Apr

REPOSITORIES: biostudies-literature